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Conserved domains on  [gi|901694072|ref|NP_001297998|]
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dixin isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 21-153 3.24e-60

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409062  Cd Length: 107  Bit Score: 197.52  E-value: 3.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 153
Cdd:cd21213   55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 628-703 3.58e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


:

Pssm-ID: 459936  Cd Length: 77  Bit Score: 133.42  E-value: 3.58e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072  628 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 703
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-496 2.99e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 307 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 386
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 387 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 466
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180       190
                 ....*....|....*....|....*....|
gi 901694072 467 EEALRKLSDASYQQVDLERELEQKDVLLAH 496
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 21-153 3.24e-60

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 197.52  E-value: 3.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 153
Cdd:cd21213   55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 628-703 3.58e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 133.42  E-value: 3.58e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072  628 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 703
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 628-704 1.39e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 83.62  E-value: 1.39e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 901694072   628 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 704
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 23-152 2.12e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 69.62  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   23 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694072  103 QQEMKSNVERVLQFvASKKIRMHQTS--AKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:pfam00307  58 EFDKLENINLALDV-AEKKLGVPKVLiePEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 24-150 2.37e-08

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 52.32  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072    24 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 103
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 901694072   104 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 150
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-496 2.99e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 307 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 386
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 387 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 466
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180       190
                 ....*....|....*....|....*....|
gi 901694072 467 EEALRKLSDASYQQVDLERELEQKDVLLAH 496
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-496 1.65e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   306 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 383
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   384 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 461
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 901694072   462 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 496
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
19-151 3.04e-06

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 50.71  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  19 SQQLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvql 98
Cdd:COG5069    8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE----------------------- 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072  99 SPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:COG5069   61 TPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRL 113
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 310-507 2.92e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   310 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 381
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   382 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 452
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   453 GQKDrlfqqqqAKLEEALRKLSDASYQQVDL-----ERELEQKDVllahcmKGETDEVTN 507
Cdd:pfam15921  614 DKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
PTZ00121 PTZ00121
MAEBL; Provisional
 302-491 2.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  302 EATWEEQLLEQQEHLEKEmEEAKKMISGLQAlllngslPEDEQERPValcEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 381
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA-EEEKKKVEQLKK-------KEAEEKKKA---EELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  382 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 454
Cdd:PTZ00121 1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 901694072  455 KDRLfqqQQAKLEEALRKLSDASYQQVDLERELEQKD 491
Cdd:PTZ00121 1756 KKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 21-153 3.24e-60

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 197.52  E-value: 3.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21213    1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 153
Cdd:cd21213   55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 628-703 3.58e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 133.42  E-value: 3.58e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072  628 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 703
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 21-151 9.01e-25

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 99.19  E-value: 9.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21212    1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAV--------------------------AGEKVPGIHSRP 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21212   55 KTRAQKLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 628-704 1.39e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 83.62  E-value: 1.39e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 901694072   628 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 704
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 21-151 1.92e-14

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 69.62  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21227    5 QKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEIL--------------------------QGRKLGRVIKKP 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21227   57 LNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 23-152 2.12e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 69.62  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   23 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 901694072  103 QQEMKSNVERVLQFvASKKIRMHQTS--AKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:pfam00307  58 EFDKLENINLALDV-AEKKLGVPKVLiePEDLVEGDNKSVLTYLASLFRRFQ 108
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 25-148 1.58e-13

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 66.98  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  25 YVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPSNQQ 104
Cdd:cd21286    5 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQII--------------------------ANEKVEDINGCPRSQS 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 901694072 105 EMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALA 148
Cdd:cd21286   59 QMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLS 102
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 20-144 4.65e-13

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 65.87  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  20 QQLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEkltgvQLS 99
Cdd:cd21214    5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVI--------------------------SGE-----RLP 51

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 901694072 100 PSNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLV 144
Cdd:cd21214   52 KPERGKMRfhkiANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMI 100
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 21-151 1.07e-12

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 64.73  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfkaagEKLTGVQLSP 100
Cdd:cd21215    5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGD--------------------------ESLGRYNKNP 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21215   57 KMRVQKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 23-148 1.71e-12

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 64.60  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  23 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPSN 102
Cdd:cd21285   13 QIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVV--------------------------ANEKIEDINGCPKN 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 901694072 103 QQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALA 148
Cdd:cd21285   67 RSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLS 112
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 22-148 7.90e-12

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 62.36  E-value: 7.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  22 LQAYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPS 101
Cdd:cd00014    1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKL--------------------------SPGSIPKINKKPK 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 901694072 102 NQQEMKSNVERVLQFVASKKI-RMHQTSAKDIVE-GNLKSIMRLVLALA 148
Cdd:cd00014   54 SPFKKRENINLFLNACKKLGLpELDLFEPEDLYEkGNLKKVLGTLWALA 102
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 21-152 7.31e-11

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 59.70  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSvKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 100
Cdd:cd21186    3 QKKTFTKWINSQLSKANK-PPIKDLFEDLRDGTRLLALLEV-------------------------------LTGKKLKP 50

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 901694072 101 ---SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21186   51 ekgRMRVHHLNNVNRALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 21-151 5.22e-10

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 57.15  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGQLALDSDASvdertdffllHSPFKAagekltgvqlsp 100
Cdd:cd21242    6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG----------HNVFQC------------ 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 snqqemKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21242   64 ------RSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHF 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 21-152 1.80e-09

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 55.49  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 100
Cdd:cd21188    4 QKKTFTKWVNKHLIK--ARRRVVDLFEDLRDGHNLISLLEVL--------------------------SGESL------P 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072 101 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21188   50 RERGRMRfhrlQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 21-152 3.30e-09

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 54.88  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21190    6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVL--------------------------SGQKLPIESGRV 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21190   60 LQRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQ 111
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 21-151 1.14e-08

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 53.25  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhSPFKAAGEKltgvqlSP 100
Cdd:cd21183    5 QANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLST-------------------RPLKRSYNR------RP 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21183   58 AFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 21-147 1.32e-08

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 53.30  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfKAAGEKLtgvQLSP 100
Cdd:cd21225    5 QIKAFTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSG----------------------KKFPKKF---DLEP 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 901694072 101 SNQQEMKSNVERVLQFVASK-KIRMHQTSAKDIVEGNLKSIMRLVLAL 147
Cdd:cd21225   59 KNRIQMIQNLHLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 21-152 1.72e-08

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 53.15  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGqlaldsdasvdertdffllhspfkaaGEKLTGVQLSP 100
Cdd:cd21241    6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLS--------------------------GEKLPCEKGRR 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21241   60 LKRVHFLSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 21-151 2.24e-08

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 52.49  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllHSPFKAagekltgvqlSP 100
Cdd:cd21228    5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRM---------------YKKYNK----------RP 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21228   58 TFRQMKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 24-150 2.37e-08

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 52.32  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072    24 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 103
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 901694072   104 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 150
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 28-147 2.53e-08

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 52.69  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  28 WVNAQLKKR-PSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasVDERTDFFLLHSPfkaagekltgvqLSPSNQQEm 106
Cdd:cd21218   18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSL----------APELCDKELVLEV------------LSEEDLEK- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 901694072 107 ksNVERVLQFVASKKIRMHqTSAKDIVEGNLKSIMRLVLAL 147
Cdd:cd21218   75 --RAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFVATL 112
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 41-151 1.08e-07

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 51.05  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  41 PVQDLRQDLRDGVilaYLIEIVGQLAldsdasvdertDFFL-LHSPFkaagekltgvqLSPSNQQEMKSNVERVLQFVAS 119
Cdd:cd21222   35 EVTDLATQFHDGV---YLILLIGLLE-----------GFFVpLHEYH-----------LTPSTDDEKLHNVKLALELMED 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 901694072 120 KKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21222   90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 21-147 1.77e-07

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 50.06  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 100
Cdd:cd21246   17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEV-------------------------------LSGERLPK 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNlksiMRLVLAL 147
Cdd:cd21246   64 PTKGKMRihclENVDKALQFLKEQRVHLENMGSHDIVDGN----HRLTLGL 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-496 2.99e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 307 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 386
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 387 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 466
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                        170       180       190
                 ....*....|....*....|....*....|
gi 901694072 467 EEALRKLSDASYQQVDLERELEQKDVLLAH 496
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 23-152 3.52e-07

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 49.66  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  23 QAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIeivGQLaldsdasvderTDFFLLHSPFkaagekltgvQLSPSN 102
Cdd:cd21307   19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLI---GQL-----------EGFFIHLSEF----------FLTPSS 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 901694072 103 QQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21307   73 TSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-495 3.67e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 301 LEATWEEqLLEQQEHLEKEMEEAKKMISGLQALLlngslpedEQERpvalcepgvnpeEQLIIIRSRLDQSVEENQDLKK 380
Cdd:COG1196  237 LEAELEE-LEAELEELEAELEELEAELAELEAEL--------EELR------------LELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 381 ELLKC-------KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELG 453
Cdd:COG1196  296 ELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 901694072 454 QKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 495
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 21-147 7.49e-07

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 48.45  E-value: 7.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 100
Cdd:cd21193   17 QKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEI-------------------------------ISGEKLGK 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 901694072 101 SNQQEMK----SNVERVLQFVASKkIRMHQTSAKDIVEGNlksiMRLVLAL 147
Cdd:cd21193   64 PNRGRLRvqkiENVNKALAFLKTK-VRLENIGAEDIVDGN----PRLILGL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
307-490 1.41e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  307 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSVEENQDLKKE 381
Cdd:COG4913   228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  382 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLEERNRLLGEYK---KELGQKD- 456
Cdd:COG4913   297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEallAALGLPLp 376

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 901694072  457 ----------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQK 490
Cdd:COG4913   377 asaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-496 1.65e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   306 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 383
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   384 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 461
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 901694072   462 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 496
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 316-489 2.36e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   316 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGI 395
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   396 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSD 475
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369

                          170
                   ....*....|....
gi 901694072   476 ASYQQVDLERELEQ 489
Cdd:TIGR02168  370 LESRLEELEEQLET 383
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
19-151 3.04e-06

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 50.71  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  19 SQQLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvql 98
Cdd:COG5069    8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE----------------------- 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072  99 SPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:COG5069   61 TPETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRL 113
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 17-151 6.85e-06

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 45.79  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  17 APSQQLQ--AYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdFFLLHSpfkaageklt 94
Cdd:cd21310   11 APWKKIQqnTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKM-----------YRKYHP---------- 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694072  95 gvqlSPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21310   68 ----RPNFRQMKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 120
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
358-488 9.96e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 358 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 427
Cdd:COG3206  204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 901694072 428 ------HNQNVDLQRKLE--------ERNRLLGEYKKE---LGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELE 488
Cdd:COG3206  284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 311-491 2.03e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   311 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 390
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   391 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 470
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180
                   ....*....|....*....|.
gi 901694072   471 RKLSDASYQQVDLERELEQKD 491
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKA 447
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-495 2.65e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  354 GVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ--DTSVLQLKQELLRANMDKDELHNQN 431
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERLDASS 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694072  432 VD---LQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 495
Cdd:COG4913   685 DDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 310-507 2.92e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.42  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   310 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 381
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   382 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 452
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   453 GQKDrlfqqqqAKLEEALRKLSDASYQQVDL-----ERELEQKDVllahcmKGETDEVTN 507
Cdd:pfam15921  614 DKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-476 4.73e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   307 EQLLEQQEHLEKEMEEAKKMISGLQAlllngSLPEDEQERPVALCEPGVNpEEQLIIIRSRLDQSVEENQDLKKELLKCK 386
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELEALLNERASL-EEALALLRSELEELSEELRELESKRSELR 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   387 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLEERNRLLGEYKKELG--------- 453
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994

                          170       180
                   ....*....|....*....|....*...
gi 901694072   454 ---QKDRL--FQQQQAKLEEALRKLSDA 476
Cdd:TIGR02168  995 yeeLKERYdfLTAQKEDLTEAKETLEEA 1022
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 307-534 4.91e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 307 EQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLK 384
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRAL--------EQELAALEAELAELEKEIAELRAELEA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 385 CKQEARNL------QGIKDALQQRLTQQDTS------------VLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLG 446
Cdd:COG4942  102 QKEELAELlralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 447 EYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMKGETDEVTNYNSHS--SQRNGFVLPVAG 524
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGfaALKGKLPWPVSG 261

                        250
                 ....*....|....*...
gi 901694072 525 R--------GATTVTHRG 534
Cdd:COG4942  262 RvvrrfgerDGGGGRNKG 279
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 26-151 7.99e-05

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409153  Cd Length: 107  Bit Score: 42.30  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  26 VAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVGQLALDsdasVDERTdffllhspfkaagekltgvQLSPSNQQE 105
Cdd:cd21304    7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLE----VAEVT-------------------QSEVGQKQK 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 901694072 106 MKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21304   62 LRTVLDKINRILNLPRWSQQKWSVDSIHSKNLVAILHLLVALARHF 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
358-489 9.17e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 9.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 358 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 437
Cdd:COG4372   44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 901694072 438 LEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 489
Cdd:COG4372  124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 27-151 1.07e-04

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 41.88  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  27 AWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEivgqlaldsdasvdertdffllhspfKAAGEKLTGVQLSPSNQQEm 106
Cdd:cd21221    8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLE--------------------------KLANEKLEVPEVAQSEEGQ- 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 901694072 107 KSNVERVLQFVaSKKIRMHQTSAKDIVEG----NLKSIMRLVLALAAHF 151
Cdd:cd21221   59 KQKLAVVLACV-NFLLGLEEDEARWTVDGiynkDLVSILHLLVALAHHY 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 21-152 1.83e-04

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 41.41  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIV-GQLALDSdasvdertdffllHSPFkaagekltgvqls 99
Cdd:cd21191    6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLsGQNLLQE-------------YKPS------------- 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072 100 pSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21191   60 -SHRIFRLNNIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQ 111
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 21-151 2.24e-04

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 41.67  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 100
Cdd:cd21311   16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVL--------------------------SGKKFPKFNKRP 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 901694072 101 SNQQEMKSNVERVLQFVAS-KKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21311   68 TFRSQKLENVSVALKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHY 119
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 302-499 2.29e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   302 EATWEEQLLEQQEHLEKEMEEAKKMISGLQAL---------LLNGSLPEDEQERPvaLCEPGVNPEEQLIIIRSRLDQSV 372
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskeDIPNLQNITVRLQD--LTEKLSEAEDMLACEQHALLRKL 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   373 EE---NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYK 449
Cdd:TIGR00618  622 QPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 901694072   450 KELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMK 499
Cdd:TIGR00618  697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 42-148 2.30e-04

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 41.04  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  42 VQDLRQDLRDGVILAYLIEIvgqLALDSDASVDertdfflLHSPfkaAGEKLtgvqlspsnqQEMkSNVERVLQFVASKK 121
Cdd:cd21223   26 VTNLAVDLRDGVRLCRLVEL---LTGDWSLLSK-------LRVP---AISRL----------QKL-HNVEVALKALKEAG 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 901694072 122 IRMHQT----SAKDIVEGNLKSIMRLVLALA 148
Cdd:cd21223   82 VLRGGDgggiTAKDIVDGHREKTLALLWRII 112
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 17-151 3.79e-04

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 41.22  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  17 APSQQLQ--AYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKlt 94
Cdd:cd21309   12 APWKKIQqnTFTRWCNEHLKCVN--KRIGNLQTDLSDGLRLIALLEVLSQKRM------------------YRKYHQR-- 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694072  95 gvqlsPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21309   70 -----PTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHY 121
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
306-489 4.26e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 306 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiiRSRLDQsVEENQDLKKELLKC 385
Cdd:COG4717  332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL---RAALEQ-AEEYQELKEELEEL 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 386 KQEarnLQGIKDALQQRLTQQDTSvlQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK--ELGQKDRLFQQQQ 463
Cdd:COG4717  408 EEQ---LEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELK 482

                        170       180
                 ....*....|....*....|....*.
gi 901694072 464 AKLEEALRKLSDASYQQVDLERELEQ 489
Cdd:COG4717  483 AELRELAEEWAALKLALELLEEAREE 508
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 17-151 4.58e-04

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 40.84  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  17 APSQQLQ--AYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKlt 94
Cdd:cd21308   15 APWKKIQqnTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKM------------------HRKHNQR-- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 901694072  95 gvqlsPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 151
Cdd:cd21308   73 -----PTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHY 124
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 24-147 4.91e-04

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 40.25  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  24 AYVAWVNAQLKKRPSVK-------PVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaageKLTGV 96
Cdd:cd21217    5 AFVEHINSLLADDPDLKhllpidpDGDDLFEALRDGVLLCKLINKI------VPGTIDER---------------KLNKK 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 901694072  97 qlSPSNQQEMKSNVERVLQfvASKKIRMHQTS--AKDIVEGNLKsimrLVLAL 147
Cdd:cd21217   64 --KPKNIFEATENLNLALN--AAKKIGCKVVNigPQDILDGNPH----LVLGL 108
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 307-488 5.18e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  307 EQLLEQQEHLEKEMEEAKKMISGLQALLLN-----GSLPE--DEQERPValcepgvnpeEQLIIIRSRLDQS-VEENQDL 378
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalTTLEEalSEKERII----------ERLKEQREREDRErLEELESL 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  379 KKELLKCKQEArnlqgikDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLEERNRLLGEYKK---- 450
Cdd:pfam10174 474 KKENKDLKEKV-------SALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahna 546

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 901694072  451 -ELGQKDRLFQQQQAKLE-EALRKLSDASYQQVDLERELE 488
Cdd:pfam10174 547 eEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVERLLG 586
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 348-495 1.33e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 348 VALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD---- 423
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieer 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 424 KDELHNQNVDLQR----------------------------KLEERNR-LLGEYKKELGQKDRLFQQQQAKLEEALRKLS 474
Cdd:COG3883   85 REELGERARALYRsggsvsyldvllgsesfsdfldrlsalsKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKA 164

                        170       180
                 ....*....|....*....|.
gi 901694072 475 DASYQQVDLERELEQKDVLLA 495
Cdd:COG3883  165 ELEAAKAELEAQQAEQEALLA 185
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 365-495 1.65e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 365 RSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRL 444
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072 445 LGE-----YKKE--------LGQKD------------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 495
Cdd:COG4942  106 LAEllralYRLGrqpplallLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 304-491 2.04e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  304 TWEEQLLE---QQEHLEKEMEEAKKmisglqalllngslpedEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDL-- 378
Cdd:pfam13851  30 SLKEEIAElkkKEERNEKLMSEIQQ-----------------ENKR---LTEPLQKAQEEVEELRKQLENYEKDKQSLkn 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  379 -KKELLKCKQEARNLQGIKDALQQRLTqqdtsvlQLKQEllranmdKDELHNQNV----DLQRKLEERNRLLgeyKKELG 453
Cdd:pfam13851  90 lKARLKVLEKELKDLKWEHEVLEQRFE-------KVERE-------RDELYDKFEaaiqDVQQKTGLKNLLL---EKKLQ 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 901694072  454 QKDRLFQQQQAKLEEALR--KLSDASYQQVD--LERELEQKD 491
Cdd:pfam13851 153 ALGETLEKKEAQLNEVLAaaNLDPDALQAVTekLEDVLESKN 194
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 307-488 2.48e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.99  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  307 EQLLEQQEHLE-----KEMEEAKKMISGLQALLLNGSLPEdeqerpvalcepgvnPEEQLIIIRSRLDQSVEenqDLKKE 381
Cdd:pfam06160 221 REMEEEGYALEhlnvdKEIQQLEEQLEENLALLENLELDE---------------AEEALEEIEERIDQLYD---LLEKE 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  382 LlkckqEARN-LQGIKDALQQRLTQQDTSVLQLKQELLRAN----MDKDELHNQNvDLQRKLEERNRLLGEYKKELGQKD 456
Cdd:pfam06160 283 V-----DAKKyVEKNLPEIEDYLEHAEEQNKELKEELERVQqsytLNENELERVR-GLEKQLEELEKRYDEIVERLEEKE 356

                         170       180       190
                  ....*....|....*....|....*....|..
gi 901694072  457 RLFQQQQAKLEEALRKLSDASYQQVDLERELE 488
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQEEFKESLQ 388
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 306-489 2.56e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  306 EEQLLEQQEHLEKEMEEAKKMISGL----QALllngslpeDEQ--------------ERPVALCE-PGVNPE---EQLII 363
Cdd:COG3096   374 AEQLAEAEARLEAAEEEVDSLKSQLadyqQAL--------DVQqtraiqyqqavqalEKARALCGlPDLTPEnaeDYLAA 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  364 IRSRLDQSVEENQDLKKEL---------------LKCK-----------QEARNLqgIKDALQQRLTQQDTSVLQLKQEL 417
Cdd:COG3096   446 FRAKEQQATEEVLELEQKLsvadaarrqfekayeLVCKiageversqawQTAREL--LRRYRSQQALAQRLQQLRAQLAE 523

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 901694072  418 LRanmdkdelhnQNVDLQRKLEernRLLGEYKKELGQK-------DRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 489
Cdd:COG3096   524 LE----------QRLRQQQNAE---RLLEEFCQRIGQQldaaeelEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 299-487 2.64e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.25  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  299 TYLEATWEEQLLEQQEHLEKEMEEAKkmISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiirSRLDQSVEENQDL 378
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTKELEDIK--MSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM----EELNKAKAAHSFV 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  379 KKELlkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQK--- 455
Cdd:pfam05483 351 VTEF---EATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqf 427

                         170       180       190
                  ....*....|....*....|....*....|..
gi 901694072  456 DRLFQQQQAKLEEALRKLSDASYQQVDLEREL 487
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQL 459
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 21-163 2.69e-03

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 38.47  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 100
Cdd:cd21235    7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVL--------------------------SGDSL------P 52

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 901694072 101 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKPGSSRTVSQGR 163
Cdd:cd21235   53 REKGRMRfhklQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
359-489 2.74e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 359 EQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQ--QDTSVLQLKQELLRANMDKDELHNQNVDLQR 436
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEE 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 901694072 437 KLEERNRLLGEYKkelgQKDRLFQQQQAKLEEALRKLSDASYQQV-DLERELEQ 489
Cdd:COG4717  154 RLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELqDLAEELEE 203
PTZ00121 PTZ00121
MAEBL; Provisional
 302-491 2.83e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  302 EATWEEQLLEQQEHLEKEmEEAKKMISGLQAlllngslPEDEQERPValcEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 381
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA-EEEKKKVEQLKK-------KEAEEKKKA---EELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  382 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 454
Cdd:PTZ00121 1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 901694072  455 KDRLfqqQQAKLEEALRKLSDASYQQVDLERELEQKD 491
Cdd:PTZ00121 1756 KKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
301-497 3.12e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  301 LEATWEE--QLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDL 378
Cdd:COG4913   257 IRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL--------EAELERLEARLDALREELDEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  379 KKELLK--------CKQEARNLQGIKDALQQRLTQQDTSVLQLKqelLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK 450
Cdd:COG4913   329 EAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEE 405

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 901694072  451 ELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ-KDVLLAHC 497
Cdd:COG4913   406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRDALAEAL 453
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 21-152 3.72e-03

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 37.70  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLsP 100
Cdd:cd21237    7 QKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEV-------------------------------LSGVKL-P 52

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 901694072 101 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21237   53 REKGRMRfhrlQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 108
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 21-152 4.03e-03

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 38.04  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072  21 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqLALDSDASVDERTDFFLLHspfkaagekltgvqlsp 100
Cdd:cd21236   18 QKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEV---LSGDTLPREKGRMRFHRLQ----------------- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 901694072 101 snqqemksNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 152
Cdd:cd21236   76 --------NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 376-495 4.65e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 376 QDLKKELLKCKQEARNLQGIKDALQQRLTQqdtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQ- 454
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 901694072 455 -KDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 495
Cdd:COG1579   86 rNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 306-489 6.04e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   306 EEQLLE-----QQEHLEKEMEEAKkmISGLQALLLngsLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKK 380
Cdd:pfam01576  109 EEQLDEeeaarQKLQLEKVTTEAK--IKKLEEDIL---LLEDQNSK---LSKERKLLEERISEFTSNLAEEEEKAKSLSK 180

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   381 elLKCKQEARnlqgIKDaLQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEernrllgEYKKELGQKDRLFQ 460
Cdd:pfam01576  181 --LKNKHEAM----ISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA-------ELRAQLAKKEEELQ 246

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 901694072   461 QQQAKLEE-------ALRKLSDASYQQVDLERELEQ 489
Cdd:pfam01576  247 AALARLEEetaqknnALKKIRELEAQISELQEDLES 282
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 306-473 6.45e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   306 EEQLLEQQEHLEKEMEEAKKMISGLQA--LLLNGSLPEDEQERPVALCEPgVNPEEQLIIIRSRLDQSVEENQDLKKELL 383
Cdd:TIGR00618  710 ETHIEEYDREFNEIENASSSLGSDLAAreDALNQSLKELMHQARTVLKAR-TEAHFNNNEEVTAALQTGAELSHLAAEIQ 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072   384 KCKQEARNLQGIKDALQQRLTQQ---DTSVLQLKQELLRAnmDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLfQ 460
Cdd:TIGR00618  789 FFNRLREEDTHLLKTLEAEIGQEipsDEDILNLQCETLVQ--EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL-T 865

                          170
                   ....*....|...
gi 901694072   461 QQQAKLEEALRKL 473
Cdd:TIGR00618  866 QEQAKIIQLSDKL 878
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
358-495 9.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 901694072 358 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 437
Cdd:COG4372   58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 901694072 438 LEERNRLLGEYKKELGQkdrlFQQQQAKLEEALRKLsDASYQQVDLERELEQKDVLLA 495
Cdd:COG4372  138 IAELQSEIAEREEELKE----LEEQLESLQEELAAL-EQELQALSEAEAEQALDELLK 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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